Peptide late-stage C(sp)-H arylation by native asparagine assistance without exogenous directing groups
There is a strong demand for novel native peptide motifs for post-synthetic modifications of peptides without pre-installation and subsequent removal of directing groups. Herein, we report an efficient method for peptide late-stage C(sp 3 )-H arylations assisted by the unmodified side chain of aspar...
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| Veröffentlicht in: | Chemical science (Cambridge) 2020-08, Vol.11 (34), p.929-9295 |
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| container_issue | 34 |
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| container_title | Chemical science (Cambridge) |
| container_volume | 11 |
| creator | Weng, Yiyi Ding, Xingxing Oliveira, João C. A Xu, Xiaobin Kaplaneris, Nikolaos Zhu, Meijie Chen, Hantao Chen, Zhuo Ackermann, Lutz |
| description | There is a strong demand for novel native peptide motifs for post-synthetic modifications of peptides without pre-installation and subsequent removal of directing groups. Herein, we report an efficient method for peptide late-stage C(sp
3
)-H arylations assisted by the unmodified side chain of asparagine (Asn) without any exogenous directing group. Thereby, site-selective arylations of C(sp
3
)-H bonds at the N-terminus of di-, tri-, and tetrapeptides have been achieved. Likewise, we have constructed a key building block for accessing agouti-related protein (AGRP) active loop analogues in a concise manner.
An efficient method for peptide late-stage C(sp
3
)-H arylations assisted by unmodified side chain of asparagine (Asn) without any exogenous directing group has been reported. |
| doi_str_mv | 10.1039/d0sc03830j |
| format | Article |
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3
)-H arylations assisted by the unmodified side chain of asparagine (Asn) without any exogenous directing group. Thereby, site-selective arylations of C(sp
3
)-H bonds at the N-terminus of di-, tri-, and tetrapeptides have been achieved. Likewise, we have constructed a key building block for accessing agouti-related protein (AGRP) active loop analogues in a concise manner.
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3
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3
)-H bonds at the N-terminus of di-, tri-, and tetrapeptides have been achieved. Likewise, we have constructed a key building block for accessing agouti-related protein (AGRP) active loop analogues in a concise manner.
An efficient method for peptide late-stage C(sp
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3
)-H arylations assisted by the unmodified side chain of asparagine (Asn) without any exogenous directing group. Thereby, site-selective arylations of C(sp
3
)-H bonds at the N-terminus of di-, tri-, and tetrapeptides have been achieved. Likewise, we have constructed a key building block for accessing agouti-related protein (AGRP) active loop analogues in a concise manner.
An efficient method for peptide late-stage C(sp
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| source | DOAJ Directory of Open Access Journals; PubMed Central Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Chemistry Peptides |
| title | Peptide late-stage C(sp)-H arylation by native asparagine assistance without exogenous directing groups |
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